Function of a retrotransposon nucleocapsid protein
| Autor: | Kristina Clemens, Suzanne Sandmeyer |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
assembly
Retroelements Retrotransposon nucleocapsid viruses nucleocapsid Retrotransposon retroelement Review Biology Retrovirus Genetics Animals Humans Guide RNA Molecular Biology Virus Assembly retrotransposon Terminal Repeat Sequences RNA food and beverages Cell Biology Reverse Transcription Nucleocapsid Proteins Ty biology.organism_classification Long terminal repeat Reverse transcriptase retrovirus Retroviridae Transfer RNA Protein Binding Developmental Biology |
| Zdroj: | Sandmeyer, Suzanne B; & Clemens, Kristina A. (2010). Function of a retrotransposon nucleocapsid protein.. RNA biology, 7(6), 642-654. doi: 10.4161/rna.7.6.14117. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/8vc019d5 |
| Popis: | Long terminal repeat (LTR) retrotransposons are not only the ancient predecessors of retroviruses, but they constitute significant fractions of the genomes of many eukaryotic species. Studies of their structure and function are motivated by opportunities to gain insight into common functions of retroviruses and retrotransposons, diverse mechanisms of intracellular genomic mobility, and host factors that diminish or enhance retrotransposition. This review focuses on the nucleocapsid (NC) protein of a Saccharomyces cerevisiae LTR retrotransposon, the metavirus, Ty3. Retrovirus NC promotes genomic (g)RNA dimerization and packaging, tRNA primer annealing, reverse transcription strand transfers, and host protein interactions with gRNA. Studies of Ty3 NC have revealed key roles for Ty3 NC in formation of retroelement assembly sites (retrosomes), and in chaperoning primer tRNA to both dimerize and circularize Ty3 gRNA. We speculate that Ty3 NC, together with P-body and stress-granule proteins, plays a role in transitioning Ty3 RNA from translation template to gRNA, and that interactions between the acidic spacer domain of Ty3 Gag3 and the adjacent basic NC domain control condensation of the virus-like particle. |
| Databáze: | OpenAIRE |
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